• Title/Summary/Keyword: 산화효소

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이달의 과학자-강원대 축산가공학과 이성기 교수

  • Korean Federation of Science and Technology Societies
    • The Science & Technology
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    • v.31 no.7 s.350
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    • pp.80-81
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    • 1998
  • 축산물의 가공과 이용에 관한 연구를 진행 하고 있는 강원대 축산가공학과 이성기 교수는 '냉동 세절돈육에서 소금이 지방산화 촉진과 항산화효소 역가에 미치는 영향'이라는 논문을 발표해 세계적인 관심을 모으고 있다. 이교수는 이러한 연구를 통해 돈육에 첨가한 소금이 냉동저장중에 지방산화를 급증시키는 반변 돈육 속에 함유된 항산화 효소들의 역가는 감소시켰다고 밝히고 있다.

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The Optimum pH of Oxidoreductases: A Comparison Between Experimental and Calculated pH Optimum (산화환원 효소의 최적 pH 예측)

  • Kim, Jin Ryeon;Yang, Ji Hye;Yu, Yeong Je
    • Journal of the Korean Chemical Society
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    • v.46 no.5
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    • pp.432-449
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    • 2002
  • For various oxidoreductases, the optimum pHs of the enzymes can be calculated using the rule based on proton transfer. Relative probability of a certain amino acid side chain to be in the water, or the relative affinity to the water was calculated using Boltzman distribution. Also, the protonated and deprotonated portions of a certain amino acid side chain were calculated using p$K_R$ of that and the effective protonated and deprotonated protions were the product of relative probability and the protonated and deproteonated protions. Where the total effective protonated portion was equal to the effective deprotonated portion of amino acid side chains, it was expected that oxidoreductases have max-imum activities. The optimum pHs calculated by our rule were compared with the experimental results.

Identification and Phylogenetic Relationship at Cytochrome Oxidase Subunit I (COI) Gene among Korean Terrestrial Planarian Taxa (한국 내 육지플라나리아 간 치토크롬 산화효소의 동정과 계통유전학적 관계)

  • Moon, Doo-Ho;Lee, Young-Ah;Huh, Man-Kyu
    • Journal of Life Science
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    • v.21 no.7
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    • pp.939-946
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    • 2011
  • Sequence data of Cytochrome Oxidase Subunit I (COI) gene of mitochondria were used to elucidate the taxonomy and phylogenetic relationships of the terrestrial planarian taxa in Korea. Published COI gene sequences from Family Bipaliidae in GenBank were also included in the phylogenetic analysis. The aligned data sets for Terricola ranged from 387 to 444 nucleotides (bp) as a result of differences in insert nucleotides. The phylogeny based on COI analysis was not congruenced with the morphological traits. Bipalium nobile included the remainder taxa (Bipalium adventitium, Bipalium venosum, Bipalium kewense, and Bipalium multilineatum). Internal nodes were strongly supported (>91%). The phylogenetic tree on COI analysis showed that most identified species were well separated from each other. The main phylogenetic analysis formed monophyletic groups. COI gene of mitochondria could have the resolving power for taxonomy information for the terrestrial planarian taxa in Korea.

Preparation of Enzyme Electrodes for Biofuel Cells Based on the Immobilization of Glucose Oxidase in Polyion Complex (폴리이온복합체를 이용하여 글루코스 산화효소를 고정화한 바이오전지용 효소전극 제조)

  • Nguyen, Linh Thi My;Li, Nan;Yoon, Hyon Hee
    • Applied Chemistry for Engineering
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    • v.24 no.1
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    • pp.99-103
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    • 2013
  • An emzymatic bioanode for a glucose/oxygen biofuel cell was prepared by the sequential coating of carbon nanotube (CNT), charge transfer complex (CTC) based on tetracyanoquinodimethane (TCNQ) and tetrathiafulvalene (TTF), glucose oxidase (GOx), and polyion complex (mixture of poly-L-lysine hydrobromide and poly (sodium 4-styrenesulfonate)) on a glassy carbon electrode. A biocathode was also prepared by the sequential coating of CNT, bilirubin oxidase (BOD), 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS), and polyion complex. The effect of CNT and CTC on the electrochemical performance was investigated. The biofuel cell exhibited a promising performance with maximum power densities of 3.6, 10.1, and $46.5{\mu}W/cm^2$ at 5, 20, and 200 mM of glucose concentration, respectively. The result indicates that the biofuel cell architecture prepared in this study can be used in the development of biofuel cells and biosensors.

Immobilization and Characterization of Rifamycin B Oxidase in Cellulose Acetate Beads (셀룰로오스 아세테이트에 고정화된 리파마이신 B 산화효소의 특성)

  • Chung, Bong-Hyun;Chang, Ho-Nam;Han, Moon-Hi
    • Microbiology and Biotechnology Letters
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    • v.13 no.2
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    • pp.115-118
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    • 1985
  • Rifamycin B oxidase converts rifamycin B to rifamycin S using oxygen as cosubstrate. Humnicola spp. (ATCC 20620) was treated with acetone and the cell powder was immobilized with cellulose acetate. The properties of the immobilized enzyme was examined. The optimum pHs of the immobilized and the free enzymes were 7.2. The optimum temperature of the immobilized enzyme was at 50-55$^{\circ}C$, which was 5$^{\circ}C$ higher than that of the free enzyme. The activities of the immobilized enzyme appeared less sensistive with respect to the changes of temperature and pH as compared to those of the free enzyme. Twenty percent of the enzyme activity was recovered when the enzyme was immobilized in 3mm beads. The storage stability was good below 4$0^{\circ}C$, but the activity decreased very rapidly above 5$0^{\circ}C$. The physical strength of the beads was good and was suitable as packing material in a three-phase enzyme reactor.

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Isolation and Identification of Probiotic Bacillus strain Forming Amine Oxidase from Traditional Fermented Soybean Paste (재래식 된장으로부터 아민 산화 효소를 생산하는 프로바이오틱 바실러스균의 분리 동정)

  • Lim, Eun-Seo
    • Journal of the Korean Applied Science and Technology
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    • v.37 no.6
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    • pp.1535-1544
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    • 2020
  • The primary objective of this study was to isolate and identify amine oxidase-producing probiotic Bacillus strains from traditional fermented soybean paste. Biogenic amines (BA)-forming bacteria isolated from the samples were identified as Bacillus sp. TS09, Bacillus licheniformis TS17, Bacillus subtilis TS19, Bacillus cereus TS23, Bacillus sp. TS30, Bacillus megaterium TS31, B. subtilis TS44, Bacillus coagulans TS46 and Bacillus amyloliquefaciens TS59. Meanwhile, B. subtilis TS04 and TS50 isolated from the same samples exhibited good probiotic properties, including the tolerance to artificial gastric juice and bile salts, the adhesion to intestinal epithelial cells, and the production of bacteriocin(s) active against BA-forming bacteria (Bacillus sp. TS30 and B. subtilis TS44). In addition, the amine oxidase produced by B. subtilis TS04 and TS50 significantly decreased the formation of BA, especially cadaverine, putrescine, and tyramine, therefore, these strains could be considered good potential probiotic candidates to prevent or reduce BA accumulation in food products.

Altered Vascular Expression of Nitric Oxide Synthase Isozymes in Hypertension (고혈압에서 혈관 산화질소 합성 동위 효소 발현 변화)

  • 김인광;강대길;이종은;오봉석
    • Journal of Chest Surgery
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    • v.32 no.2
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    • pp.138-143
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    • 1999
  • Background: The endothelium-dependent vasorelaxation has been largely accounted for by the release of nitric oxide (NO). Three distinct isoforms of NO synthases (NOS) have been characterized, i.e., brain(bNOS), inducible (iNOS), and endothelial constitutive (ecNOS). Although hypertension hasbeen associated with a vascular endothelial dysfunction, changes in the vascular expression of NOS isoforms have not been established. The present study was aimed at exploring the vascular expression of NOS isozymes in hypertension. Material and Method: Two-kidney, one clip (2K1C) and deoxycorticosterone acetate (DOCA)-salt hypertension were induced in rats. The expression of different NOS isozymes in the thoracic aorta was determined by Western blot analysis. The vascular tissue contents of nitrites were measured by colorimetric assay. Result: Arterial blood pressure was significantly higher in experimental groups of 2K1C and DOCA-salt rats compared with their corresponding control rats. The vascular expression of bNOS as well as that of ecNOS was decreased in both models of hypertension. iNOS was not changed in DOCA-salt hypertension, but was also decreased in 2K1C hypertension. The vascular contents of nitrites were significantly decreased in DOCA-salt as well as in 2K1C hypertension. Conclusion: These results suggest that 2K1C and DOCA-salt hypertension are associated with decreases in the vascular expression of NOS isozymes and nitrite contents.

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The Concentration and Purification of Enzyme by Ultrafiltration Membrane (한외여과막을 이용한 효소의 정제, 농축)

  • 장재영;김정학;황기호;김기협;정인범
    • Proceedings of the Membrane Society of Korea Conference
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    • 1994.04a
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    • pp.26-27
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    • 1994
  • 효소는 생체내의 합성, 분해, 산화, 환원 등 복잡한 화학반응이 상온, 상압, 중성부근에서 효율적으로 진행되게 하는 단백질이 주성분인 유기촉매이다. 현재 알려져 있는 효소의 종류는 수백만종 이상으로 추정되며 그 중 100여종 이상은 순수한 결정상태이며 약 600종 정도는 어느 정도 순수하게 징제되고 있다. 이들 효소의 분자량은 Ribonuclease의 12,700에서 부터 L-Glutamate dehydrogenase나 Carboxylase의 1,000,000 이상으로 광범위하다.

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Properties of Ascorbate-Oxidizing Enzyme Purified from Pleurotus ostreatus (Pleurotus ostreatus에서 분리한 아스콜빈산 산화효소의 특성)

  • 황윤엽;김연란;강사욱
    • Korean Journal of Microbiology
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    • v.26 no.4
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    • pp.324-331
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    • 1988
  • Ascorbate oxidizing enzyme from the crude extract of Pleurotus ostreatus was purified by ammonium sulfate precipitation, preparative polyacrylamide gel electrophoresis, DEAE Sepharose CL-6B ion exchange chromatography and Sephadex G-150 gel filtration chromatography. The molecular weight of the enzyme estimated by Sephadex G-150 gel filtration chromatography was 140,000 and that of its subunit by SDS-polyacrylamide gel electrophoresis 66,000. The optimum pH for the maximum activity of the enzyme was 5.2 and the isoelectric point of the enzyme was 6.0 Km values for L-ascorbic acid and D-isoascorbic acid were both 2.2.$\mu$M, which indicates that the enzyme has the asme affinity towards both substrates.

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